A direct comparison of protein structure in the gas and solution phase: the Trp-cage

Alexandra Patriksson, Christopher M Adams, Frank Kjeldsen, Roman A Zubarev, David van der Spoel

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Molecular dynamics simulations of zwitterions of the Trp-cage protein in the gas phase show that the most stable ion in vacuo has preserved the charge locations acquired in solution. A direct comparison of the gas and solution-phase structures reveals that, despite the similarity in charge location, there is significant difference in the structures, with a substantial increase in hydrogen bonds and exposure of hydrophobic parts in the gas phase. The structure of the salt bridge in the gas phase is also much more stable than in the (experimental) solution structure.
Original languageEnglish
JournalJournal of Physical Chemistry B
Volume111
Issue number46
Pages (from-to)13147-13150
Number of pages3
ISSN1520-6106
DOIs
Publication statusPublished - 22. Nov 2007

Keywords

  • Gases
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Peptides
  • Protein Conformation
  • Solutions

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